biostudies-literatureSundermeyer LDeutsche ForschungsgemeinschaftAgence Nationale de la RechercheHeinrich-Heine-Universität Düsseldorfe0267722https://www.ebi.ac.uk/biostudies/studies/S-EPMC9769921biostudies-literatureUnknown10(6)In Corynebacterium glutamicum the protein kinase PknG phosphorylates OdhI and thereby abolishes the inhibition of 2-oxoglutarate dehydrogenase activity by unphosphorylated OdhI. Our previous studies suggested that PknG activity is controlled by the periplasmic binding protein GlnH and the transmembrane protein GlnX, because Δ<i>glnH</i> and Δ<i>glnX</i> mutants showed a growth defect on glutamine similar to that of a Δ<i>pknG</i> mutant. We have now confirmed the involvement of GlnH and GlnX in the control of OdhI phosphorylation by analyzing the OdhI phosphorylation status and glutamate secretion in Δ<i>glnH</i> and Δ<i>glnX</i> mutants and by characterizing Δ<i>glnX</i> suppressor mutants. We provide evidence for GlnH being a lipoprotein and show by isothermal titration calorimetry that Microbiology spectrumCharacteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum.PMC9769921ANR-18-CE92-0003BO 903/4-1iGRADbio graduate programBrocker MBosco GGujar SBott MSundermeyer LWillbold DBellinzoni MBaumgart MWeiergraber OHfalseCharacteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum.In Corynebacterium glutamicum the protein kinase PknG phosphorylates OdhI and thereby abolishes the inhibition of 2-oxoglutarate dehydrogenase activity by unphosphorylated OdhI. Our previous studies suggested that PknG activity is controlled by the periplasmic binding protein GlnH and the transmembrane protein GlnX, because Δ<i>glnH</i> and Δ<i>glnX</i> mutants showed a growth defect on glutamine similar to that of a Δ<i>pknG</i> mutant. We have now confirmed the involvement of GlnH and GlnX in the control of OdhI phosphorylation by analyzing the OdhI phosphorylation status and glutamate secretion in Δ<i>glnH</i> and Δ<i>glnX</i> mutants and by characterizing Δ<i>glnX</i> suppressor mutants. We provide evidence for GlnH being a lipoprotein and show by isothermal titration calorimetry that 2022-01-01T00:00:00Z2022 Dec2026-06-12T09:50:54.513Z2025-04-05T14:54:56.648ZS-EPMC97699213644515310.1128/spectrum.02677-22